Publication for Mpc1 and Mpc2

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Mpc1	mitochondrial pyruvate carrier 1	55951			[link]
mmu	Mpc2	mitochondrial pyruvate carrier 2	70456

Pubmed ID	Priority	Text
30356033	0.99	MPC1 and MPC2 knockdown in MEFs upregulated the ratio of lactate to pyruvate, indicating an increased free NADH level in the cytosol and nucleus.
	0.98	MPC1 and MPC2 and transcriptionally repressed them, leading to increased levels of free NADH in the cytosol and nucleus, thus positively feeding back CtBP1's functions.
	0.98	MPC1 and MPC2 are principal mediators that link CtBP1-mediated transcription regulation to NADH production.
	0.98	MPC1 and MPC2 to the MEFs cells and found that additional expression of MPC1 and MPC2 decreased their lactate-to-pyruvate ratio (Figure 1B, 1C), suggesting that the mitochondrial pyruvate transport is a key step in metabolic reprogramming that affects NADH in the cytosol and nucleus.
	0.98	MPC1 or MPC2 expression alone localized to the mitochondrial, both MPC1 and MPC2 are required for restoring the normal lactate-to-pyruvate ratio, reflecting the obligated oligomerization of the 2 components of the mitochondrial pyruvate carrier in redox maintenance.
	0.98	MPC1 and the MPC2 genes (Figure 2B).
	0.98	MPC1 and the MPC2 transcription.
	0.98	MPC1 and the MPC2 mRNA levels and protein levels were increased (Figure 3A), confirming the key role of CtBP1 in regulating MPC1 and MPC2 transcription.
	0.98	MPC1 and MPC2 genes (Figure 4B).
	0.98	MPC1 or MPC2 (Figure 4C), similar to the effect of the CtBP1 knockdown in melanoma cells (Figure 3A), suggesting that ablation of CtBP1's activity by blocking NADH rescues the MPC1 and MPC2 expression.
	0.98	MPC1 and MPC2 in melanoma cell lines, A375 and SK-MEL-28, inhibited their growth, migration, and invasion.
	0.98	MPC1 and MPC2 forces the pyruvate from the glycolytic influx to the lactate conversion, leading to increased free NADH in the cytosol and nucleus.
	0.98	MPC1 and MPC2 genes, and the CtBP1-NADH 'avalanche', and led to cell tumorigenesis by transcriptional and metabolic reprogramming.
	0.98	MPC1 and MPC2 are transcriptionally repressed by CtBP1 and thus provide positive feedback to CtBP1's functions.
	0.98	MPC1 and MPC2 inhibit melanoma cell proliferation and migration, suggesting the potential tumor-suppressor roles of MPC1 and MPC2 in melanoma cells.
	0.98	MPC1 and MPC2 genes through the regulatory regions on their gene.
	0.98	MPC1 and MPC2 promoters in A375 cells.
	0.98	MPC1 and MPC2 promoters.
	0.97	MPC1 and MPC2 in Melanoma Cells
	0.97	MPC1 and MPC2), which contribute to redox homeostasis and are transcriptionally regulated by CtBP1.
	0.97	MPC1 and MPC2 expression.
	0.97	MPC1 and MPC2 in human tumor cells decreases free NADH and inhibits melanoma cell proliferation and migration.
	0.97	MPC1 and MPC2 is found in a variety of cancers, and low MPC1 expression levels in colon cancer, kidney cancer, and lung cancer are associated with poor survival.
	0.97	MPC1 mRNA level as well as the MPC2 mRNA level (Figure 2A).
	0.97	MPC1 and the MPC2 were decreased by the hypoxia treatment (Figure 3D).
	0.97	MPC1 and MPC2 enhanced proliferation, migration and invasion of melanoma cells.
	0.97	MPC1 and MPC2 genes.
	0.97	MPC1 and MPC2 inhibits cancer cell proliferation, migration, invasion, and stemness in many types of cancer cell.
	0.97	MPC1 and MPC2 expression, our study investigated the transcriptional control of these key players in metabolic regulation, and provides another regulatory pathway intimately linked to the metabolic alterations (feed-forward).
	0.97	MPC1 and MPC2, providing a new clue to understand how MPC1 and MPC2 expression is regulated in melanoma cells.
	0.97	MPC1 or MPC2 increased the lactate/pyruvate ratio in MEFs.
	0.97	MPC1 and MPC2.
	0.97	MPC1 and MPC2 mRNA expression.
	0.97	MPC1 and MPC2 repression mediated by CtBP1.
	0.97	MPC1 and MPC2 mRNA and protein expression.
	0.97	MPC1 and MPC2 genes.
	0.97	MPC1 and MPC2 or 2-DG treatment inhibited melanoma cell invasion.
	0.96	MPC1 and MPC2 repression in melanoma cells
	0.96	MPC1 and MPC2 expression repressed malignant properties of melanoma cells
	0.96	MPC1 and MPC2 mRNA and protein expression.
	0.95	MPC1 and the MPC2 genes in melanoma cells.
	0.95	MPC1 and MPC2 knockdown.
	0.95	MPC1 and MPC2 promoted melanoma cell invasive ability.
	0.94	MPC1 and MPC2 expression
	0.94	MPC1 and MPC2 expression in melanoma cells
	0.93	MPC1 and MPC2 transcription control.
	0.93	MPC1 or MPC2 is lethal for mouse embryo development.
	0.92	MPC1 and the MPC2 genes is subject to NADH control.
	0.92	MPC1 or MPC2 by CtBP1 is subject to NADH regulation, we investigated whether NADH blockage can be used for rescuing the MPC1 or MPC2 expression in melanoma cells.
	0.92	MPC1 and MPC2 to MEFs cells decreased lactate/pyruvate ratio.
	0.90	MPC1 and MPC2 are required for cellular redox homeostasis
	0.86	MPC1 and MPC2 in melanoma cells, we assayed melanoma cells growth and migration upon expression or knockdown of MPC1 and MPC2.
	0.85	MPC1 and MPC2 are regulated in cancer cells still remains unknown.
	0.82	MPC1 and MPC2 did not further increase the lactate-to-pyruvate ratio, suggesting that MPC1 and MPC2 work in a functional unit (Figure 1A).
	0.75	MPC1 and MPC2 in A375 and SK-MEL-28 cells.
	0.67	MPC1 and MPC2 promoter.
27835892	0.98	MPC1 and MPC2 which mounting in the inner mitochondrial membrane and it facilitates pyruvate into the mitochondrial matrix.
	0.97	MPC1 and MPC2 protein expressions were present in multiple tissues of the wild type C57BL/6J mice (Figure 1A, 1B).
	0.97	MPC1 and MPC2 were also verified in all tissues with quantitative RT-PCR (Figure 1C), suggesting a fundamental role of MPC in mice.
	0.97	MPC1 and MPC2 have two transmembrane alpha helixes in the mitochondrial membrane, which together constitute a heterodimer.
	0.96	MPC1 and MPC2 in different organs.
	0.93	MPC1 and MPC2 in the liver of the MPC1 mutation mice also revealed protein expression differences.
	0.91	MPC1 and MPC2.
	0.89	MPC1 and MPC2 play the same role in the pyruvate cellular transportation in mice.
	0.85	MPC1 heterozygous mutation mice mating experiments have confirmed the reduced fertility capacity, which is consistent with the lethal MPC2 deletion in embryos.
	0.75	MPC2 protein expression in the MPC1 heterozygous and homozygous mice was also correspondingly decreased.
	0.72	MPC1 and MPC2 is largely characterised, the importance of MPC1 gene mutations in vivo is still a matter of studies.
26344103	0.98	Mpc1 and Mpc2 proteins is required for efficient regulation of hepatic gluconeogenesis.
	0.98	Mpc1 and Mpc2 proteins are expressed at relatively high levels in the liver, the major site of gluconeogenesis (Figure 1A).
	0.98	Mpc1 but not Mpc2 transcript abundance increased with diet-induced obesity (Figure 6D).
	0.98	Mpc1 and Mpc2 protein increased (Figure S5B), raising the possibility that the increased Mpc1 protein stabilizes and post-transcriptionally increases levels of Mpc2 protein.
	0.97	Mpc1 and Mpc2 protein, with smaller or no increases in markers of the mitochondrial respiratory chain (Figure 6E).
	0.96	Mpc1 protein was accompanied by loss of Mpc2 protein (Figure 1C), because Mpc1 protein is required for stable expression of Mpc2 protein, and therefore loss of the MPC protein complex.
	0.95	Mpc1 and Mpc2 genes to a fundamental in vivo function at the intersection of cytosolic and mitochondrial metabolism.
	0.94	MPC1 and MPC2 associate in a heteroligomer of currently unknown but possibly dynamic stoichiometry.
	0.94	Mpc1 LivKO mitochondria was not amplified by treatment with the MPC inhibitor 4-alpha-hydroxycinnamatic acid (CHC) and matched that for WT mitochondria treated with CHC, both consistent with inhibition of the Mpc1-Mpc2 complex by CHC.
	0.94	Mpc1 and Mpc2 genes (MPC) for hepatic gluconeogenesis.
24910426	0.98	MPC1 and MPC2, which form a hetero-oligomeric complex in the inner mitochondrial membrane and that both proteins are required for complex activity and stability.
	0.98	MPC1 and MPC2 are expressed in beta cells as demonstrated by colocalization with insulin in immunohistochemical staining of pancreatic sections (Figure 6A).
	0.98	MPC1 and MPC2 proteins are expressed in isolated pancreatic islets and demonstrated that the expression of the MPC2Delta16 protein was markedly reduced compared to WT MPC2 (Figure 6B).
	0.98	MPC1 and MPC2 must be coexpressed for proper assembly of the multimeric MPC complex and that depletion of either protein leads to reduced abundance of the other.
	0.97	MPC1 protein, likely reflecting the maintenance of a stoichiometric ratio of MPC1 and MPC2 protein in the complex.
	0.97	MPC1 protein, suggesting that the interaction between the two proteins is significantly weakened by the loss of these 16 amino acids of MPC2 (Figure 2B).
	0.97	MPC1 was only modestly affected by MPC2 truncation in BAT and islets, suggesting tissue-specific regulation of MPC complex stability or the possibility of homodimeric MPC protein complexes.
	0.78	MPC1, MPC2, pyruvate carboxylase (PC), and pyruvate dehydrogenase complex (PDH) protein in mitochondrial lysates of various tissues from Mpc2Delta16 mice and WT controls.
	0.71	Mpc2+/-) mice demonstrated only a modest reduction in MPC2 and MPC1 protein compared to WT controls (Supplemental Figure 2B).
25458843	0.98	MPC1 and MPC2, encode the multimeric mitochondrial pyruvate carrier (MPC) complex embedded in the mitochondrial inner mitochondrial membrane.
	0.98	Mpc1KD or Mpc2KD (Mpc1/2KD) cells, as this metabolite is generated predominantly from pyruvate-derived AcCoA under normal growth conditions.
	0.98	Mpc1 or Mpc2 increase oxidative glutamine metabolism to maintain flux through the TCA cycle.
	0.97	Mpc1 and Mpc2 in Lactococcus lactis induced a fourfold increase in pyruvate uptake.
	0.97	MPC1 and MPC2.
	0.95	Mpc1 and Mpc2 (Figures 1C-1D).
	0.87	Mpc1 or Mpc2 abrogated expression of both proteins, as observed previously.
	0.85	MPC1 and MPC2 as components of the mitochondrial pyruvate transporter.
	0.72	Mpc1 (Mpc1KD), Mpc2 (Mpc2KD), or control sequences (Control).
27176894	0.98	MPC1 and MPC2, which form a multimeric complex of so far unknown stoichiometry to mediate pyruvate transport across the inner mitochondrial membrane.
	0.98	MPC2 hypomorphic allele, liver-specific knock-outs of MPC1 or MPC2, acute MPC inhibition by UK5099), which showed defects in glucose-stimulated insulin secretion or gluconeogenesis, thus demonstrating a role for the MPC in regulating whole-body glucose homeostasis.
	0.98	MPC1 nor MPC2 could be detected in the MPC1gt/gt derived cells (Fig 2E), suggesting that in the absence of MPC1, MPC2 is unstable and is degraded, as previously proposed by others.
	0.97	MPC1 gene expression in MPC1gt/gt MEFs by transduction with lentiviral particles containing a MPC1-Flag fusion construct led to reexpression of both MPC1 and MPC2 proteins (Fig 2E) and a concomitant increase in pyruvate-driven OCR compared to the parental MPC1gt/gt MEFs (Fig 2F and 2G).
	0.94	MPC1gt/gt embryos (Fig 6C and 6D) while Vigueira et al. reported increased lactate in the blood of the MPC2 hypomorphic mutant.
	0.93	MPC1gt/gt primary MEFs had very low levels of MPC1 mRNA compared to MPC1+/+ MEFs, whereas MPC2 mRNA levels were unchanged (Fig 2A).
	0.85	MPC1 nor MPC2 could be detected by Western blotting in MPC1gt/gt MEFs (Fig 2E) and that no residual pyruvate import was detected making unlikely the existence of MPC-independent pyruvate import activities in these cells (Fig 2D).
	0.80	MPC1 resulted in embryonic lethality between E12 and E14 (Fig 4A and 4B), and this is consistent with the results on the MPC2 knock-out mice reported by Vigueira et al. who observed embryonic lethality around E11.
	0.63	MPC2 knock-out embryos as compared to the MPC1gt/gt embryos.
28624784	0.98	MPC1 or MPC2 in embryonic stem cells have shown that MPC may modulate the pyruvate metabolism and that may be important for the maintenance of stem cell population.
	0.97	MPC1 and MPC2 in colorectal cancer cell lines decreased cell growth in spheroids, decreased tumor size in subcutaneous xenografts, and the expressions of the stem cell markers ALDH, Lin28A, LGR5, and NANOG were suppressed in the MPC1 and MPC2 overexpression cells.
	0.96	MPC2 gene mutation led to marked reduction in both MPC1 and MPC2 protein expression.
	0.95	MPC1 and MPC2 were originally known as BRP44L and BRP44, which form a heterologous protein complex in the inner membrane of mitochondria.
	0.93	MPC1 gene knockout in this cell model resulted in deficient protein expression of MPC2, which is in line with the previous findings.
	0.93	MPC1 and MPC2 proteins in the WT prostate cancer cells by IF and Western blotting.
	0.91	MPC1 gene knockout mouse cells express neither MPC1 nor MPC2 protein.
	0.67	MPC1 protein expression was completely disappeared in contrast to the parental cells, while the MPC2 protein expression was also reduced as shown in Figure 1B, where MT-CO1 was used as a mitochondrial locator.
28597936	0.98	Mpc2Delta16 mice have a reduced abundance of both MPC1 and MPC2 protein compared to WT mice, but the remaining truncated MPC2 protein does properly localize to the inner mitochondrial membrane.
	0.98	MPC1 and MPC2 (Figure 5A).
	0.98	MPC1 and MPC2).
	0.97	MPC1 and MPC2 protein abundance as well (Figure 5B).
	0.93	MPC1 and MPC2, comprise the MPC complex.
	0.92	MPC1 and MPC2, which form a heteroligomeric complex.
	0.86	MPC2, which destabilizes the MPC complex and essentially leads to double deletion of MPC1 and MPC2 protein, leads to early embryonic lethality in mice.
26344101	0.98	MPC2 and MPC1 proteins in LS-Mpc2-/- liver (Figures 1C, D), which is consistent with previous studies suggesting that both proteins are required for MPC complex stability.
	0.98	Mpc1 and Mpc2, in the liver with no differences between fl/fl and LS-Mpc2-/- mice other than the loss of Mpc2 (Figure 3B).
	0.97	MPC1 or MPC2 destabilizes the MPC complex and leads to loss of both proteins.
	0.97	LS-Mpc2-/- mice detected significant impairments in hepatic mitochondrial pyruvate metabolism and gluconeogenesis that were similar to mice with liver-specific deletion of the other protein of the MPC complex, MPC1 (Gray et al., co-submitted).
	0.97	Mpc1 and Mpc2 mRNA and protein in fl/fl mice (Figure 4D).
	0.95	Mpc2 mRNA was dramatically reduced in LS-Mpc2-/- liver compared to controls, while Mpc1 and Mpc2 mRNA remained unaltered in kidney and intestine, consistent with liver-specific Mpc2 deletion (Figure 1B).
25748677	0.98	MPC1/MPC2 proteins are highly expressed in BAT compared with other mouse tissues, even when corrected for mitochondrial protein content.
	0.97	MPC1 and MPC2 in Lactococcus lactis was sufficient to facilitate pyruvate import into the bacterium, and this transport was sensitive to UK-5099.
	0.97	MPC1 or MPC2 sensitized cells to the thiazolidinedione-mediated inhibition of pyruvate respiration.
	0.94	MPC1/MPC2 expression in both mouse heart and mouse liver, and also observed a 30% decrease in pyruvate-stimulated respiration in heart mitochondria from mice with a truncated MPC2 protein.
27656398	0.98	MPC1 and MPC2), which form a hetero-oligomeric complex in the IMM.
	0.98	MPC1 or MPC2 leads to destabilization and degradation of the complex, effectively resulting in a MPC double knockout and significantly reduced mitochondrial pyruvate uptake.
	0.93	Mpc1 or Mpc2 in the liver of mice leads to hypoglycemia and protects mice from the development of diabetes.
	0.90	MPC1 or MPC2 in mice leads to lethality at early embryonic stages.
28659972	0.98	Mpc1 and Mpc2, serves as the channel to facilitate pyruvate transport across the impermeable mitochondrial membrane.
	0.96	Mpc1 or Mpc2 in flies or preincubation with a specific pyruvate transport inhibitor (UK5099) can block the cross-linking of mitochondrial membranes by TZD probes.
	0.94	Mpc1 and Mpc2 as part of a multisubunit complex, along with other unidentified proteins that may vary depending on the cell type.
29555207	0.98	MPC1 and MPC2 is sufficient to reduce stem cell proliferation, consistent with previous reports that expression of these two genes together establishes a function MPC complex and increases mitochondrial pyruvate uptake.
	0.98	MPC1 and MPC2 displayed reduced size, consistent with impaired stem cell proliferation.
	0.98	MPC1 and MPC2 to alter the cellular metabolic program.
26895100	0.98	MPC1 has been shown in many cancers, and co-expression of MPC1 and MPC2 inhibits colon cancer cell growth.
	0.97	MPC2, which could form functional transporter complexes with the ectopically expressed MPC1.
27558664	0.98	Mpc1 and Mpc2 share responsibilities for mitochondrial pyruvate transmembrane transport in fission yeast, suggesting that cells lacking Mpc2 suffer a partial defect in mitochondrial oxidative phosphorylation that results in As/Cd sensitivity.
	0.98	MPC1 or MPC2 in cancer cells impaired anchorage-independent growth.
29928345	0.98	MPC1 and MPC2 form a complex that transports pyruvate into mitochondria for further ATP production.
	0.97	MPC1 and MPC2-and existing research indicates that the MPC gene is downregulated in a variety of tumors, including colon, kidney and prostate cancer, and is closely associated with prognosis.
30093307	0.98	MPC1 and MPC2, which form a hetero-oligomeric complex in the inner mitochondrial membrane, and both proteins are required for the complex stabilize and full activity.
	0.96	MPC1 and MPC2, and the increased MPC1 expression in diabetes is responsible for hyperglycemia.
30397542	0.98	Mitochondrial pyruvate carrier 1 (MPC1) is a component of the MPC1/MPC2 heterodimer that facilitates the transport of pyruvate into mitochondria.
	0.98	MPC1 is a component of the MPC1/MPC2 complex that facilitates the transport of pyruvate into mitochondria.
22628558	0.98	MPC1 or MPC2 in mammalian cells impairs pyruvate oxidation.
27269731	0.98	Mpc1 and Mpc2 liver-specific knockout mice demonstrated a pyruvate-alanine cycling mechanism to circumvent loss of MPC activity in order to maintain gluconeogenic flux.
27270434	0.98	MPC1 and MPC2, and in cancer cells their expression modulates pyruvate oxidation.
27396958	0.98	MPC1 and MPC2, each of which is essential for its function.
27760309	0.98	Mpc1 and Mpc2) and enzymes catalyzing the conversion from pyruvate to acetyl-coenzyme A (CoA) (e.g., Dlat and Pdhx), were decreased in Lsd1cKO mice (Figure 4B; Figure S4G).
28027586	0.98	MPC1 and MPC2, that form a carrier complex in the inner mitochondrial membrane.
28218289	0.98	Mpc1 and Mpc2, were reduced in Nrg1alpha-overexpressing livers (Fig. 2d).
28812580	0.98	Mpc1, as a heterodimer with Mpc2, forms the mitochondrial pyruvate carrier MPC, a transporter on the inner mitochondrial membrane required for pyruvate entry into the mitochondria.
28851515	0.98	MPC1/MPC2), which affect pyruvate uptake into mitochondria, are increased by CHIP loss.
29153407	0.98	Mpc1 and Mpc2, whose products form a heterodimer that transports pyruvate into the mitochondria (Figure 1G).
29472561	0.98	MPC2 or the knockout of MPC1, which in turn also lead to the instability of MPC2 at a post-translational level.
30874356	0.98	MPC1 and MPC2 is the target of UK5099, and each subunit is critical for carrying cytoplasmic pyruvate into the inner matrix of the mitochondria .
31596236	0.98	MPC1 (an obligate binding partner of MPC2).
31484072	0.97	MPC1 and MPC2 in TCGA HCCs suggested the MPC may have a yet-to-be-discovered pro-tumorigenic function.
	0.93	Mpc1 and Mpc2 protein in MPC LivKO livers (Figures 2G and S2A).
	0.84	MPC1 and MPC2.
	0.80	MPC1-expressing and the highest median MPC2-expressing tumor type (Figures 1A and 1B).
27987376	0.97	MPC1 resulted in a concomitant reduction in MPC2 protein levels and vice versa (Fig. 3A, B).
	0.93	MPC1/2-silenced cells is bypassed by its cytosolic transamination to, and subsequent mitochondrial uptake of, alanine or malate, we investigated whether pyruvate metabolism was more severely compromised in isolated mitochondria from MPC2-silenced cells.
	0.70	MPC1 and MPC2 have normal glucose tolerance, fasting glucose, and rates of hepatic glucose appearance Ra in vivo.
27911865	0.97	MPC1 and MPC2 in a series of 157 esophageal squamous cell carcinomas and found that the low expression of MPC1 predicted an unfavorable outcome, indicating the regulation of metabolic reprogramming by MPC1 is pivotal for tumor cell growth.
31024553	0.97	Mpc1 and Mpc2 in vitro reduces the survival of memory plasma cells significantly.
29403375	0.96	MPC1 and MPC2 genes (also known as BRP44L and BRP44, respectively) are weakly expressed in ESCs and their expression increases during differentiation [e.g., into cardiomyocytes, MPC1, p = 4.8E-6 and MPC2 p = 6.3E-5 or into neural cells (MPC1, p < 0.0001; MPC2, p = 0.0061) ].
	0.95	MPC1 and MPC2 in colorectal cancer cell lines decreased cell growth in spheroids and reduced tumor size in subcutaneous xenografts.
31305240	0.96	MPC1and MPC2 proteins in MPC SkmKO mouse muscles (Figure 1B).
	0.83	Mpc1 but not Mpc2 transcript in MPC skmKO skeletal muscle.
31665641	0.96	Mpc1KI/+ dams exhibited a 50% reduction and Mpc1KI/KI fetuses exhibited undetectable Mpc1 and Mpc2 protein expression in liver in both the fed and fasted states (Figure 1A).
27852261	0.95	MPC1 and MPC2 expression in the DU145 cell line was identified.
	0.95	MPC1 and MPC2.
	0.95	MPC1 or MPC2 in these cell lines indicates a potential clinical role of MPC in PCA.
	0.93	MPC1 and MPC2 proteins.
	0.85	MPC1 and MPC2 in prostate cancer cell lines
26413751	0.95	MPC1 and MPC2 expressions in LnCap cells may indicate rather better mitochondrial function in these cells compared to the DU145 and PC3 cells, since both DU145 and PC3 cells are more malignant than LnCap cells.
26590711	0.95	MPC1 and MPC2 into tumor cells promoted pyruvate oxidation with no obvious effects on growth in adherent culture.
30801869	0.95	MPC1 often shows low expression in many carcinomas compared to normal cells and MPC2 tends to be highly expressed.6 It is also known that low MPC1 expression in colon cancer, renal cell carcinoma, and lung cancer has poor survival.6 In contrast, the effects of changes in the expression of the MPC subtype on the tumor are still poorly understood.
31198906	0.95	MPC1 and MPC2 protein with the exception of one pair (arrow) in which the castrate tumor harbored increased expression of MPC subunits concomitant with the emergence of the recognized constitutively active AR splice variant, AR-V7 (Fig. 2d).
25458841	0.93	MPC1 and MPC2 accumulated in all cell lines (Figure 2A).
	0.85	MPC1 and MPC2 in colon cancer cells and assessed their metabolic and proliferative phenotypes.
31242425	0.90	Mpc1 and Mpc2.
24244496	0.89	mpc1 or mpc2 cells (Fig. 6C).
29107293	0.82	Mpc1 and Mpc2 proteins with MPC LivKO (Figure S1D).
24280073	0.76	MPC1 and MPC2 in Lactococcus lactis and showed that the two genes could confer pyruvate uptake, but neither gene alone had any effect.
23650507	0.72	Mpc2 and Mpc1 (red) are present in both beta-cells (green) and other cell types.
31540439	0.71	MPC1 or MPC2 in mouse resulted in embryonic lethality.